1abv
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1abv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1abv RCSB], [http://www.ebi.ac.uk/pdbsum/1abv PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1abv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1abv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1abv RCSB], [http://www.ebi.ac.uk/pdbsum/1abv PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ATPD_ECOLI ATPD_ECOLI]] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.[HAMAP-Rule:MF_01416] This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction.[HAMAP-Rule:MF_01416] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:21, 25 December 2014
N-TERMINAL DOMAIN OF THE DELTA SUBUNIT OF THE F1F0-ATP SYNTHASE FROM ESCHERICHIA COLI, NMR, MINIMIZED AVERAGE STRUCTURE
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